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X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant.
J Biochem. 2001 Jul; 130(1):107-18.JB

Abstract

In order to elucidate the mechanism of the thermostability of proteins from hyperthermophiles, X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus (PfPCP), and its mutant protein with Ser substituted at Cys142 and Cys188 were determined at 2.2 and 2.7 A resolution, respectively. The obtained structures were compared with those previously reported for pyrrolidone carboxyl peptidases from a hyperthermophilie, Thermococcus litoralis (TlPCP), and from a mesophile, Bacillus amyloliquefaciens (BaPCP). The PfPCP structure is a tetramer of four identical subunits similar to that of the TlPCP and BaPCP. The largest structural changes among the three PCPs were detected in the C-terminal protrusion, which interacts with that of another subunit. A comparison of the three structures indicated that the high stability of PfPCP is caused by increases in hydrophobic interactions and hydrogen bonds, the formation of an intersubunit ion-pair network, and improvement to an ideal conformation. On the basis of the structures of the three proteins, it can be concluded that PfPCP does not have any special factors responsible for its extremely high stability and that the conformational structure of PfPCP is superior in its combination of positive and negative stabilizing factors compared with BaPCP.

Authors+Show Affiliations

Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11432786

Citation

Tanaka, H, et al. "X-ray Crystalline Structures of Pyrrolidone Carboxyl Peptidase From a Hyperthermophile, Pyrococcus Furiosus, and Its Cys-free Mutant." Journal of Biochemistry, vol. 130, no. 1, 2001, pp. 107-18.
Tanaka H, Chinami M, Mizushima T, et al. X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant. J Biochem. 2001;130(1):107-18.
Tanaka, H., Chinami, M., Mizushima, T., Ogasahara, K., Ota, M., Tsukihara, T., & Yutani, K. (2001). X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant. Journal of Biochemistry, 130(1), 107-18.
Tanaka H, et al. X-ray Crystalline Structures of Pyrrolidone Carboxyl Peptidase From a Hyperthermophile, Pyrococcus Furiosus, and Its Cys-free Mutant. J Biochem. 2001;130(1):107-18. PubMed PMID: 11432786.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus, and its cys-free mutant. AU - Tanaka,H, AU - Chinami,M, AU - Mizushima,T, AU - Ogasahara,K, AU - Ota,M, AU - Tsukihara,T, AU - Yutani,K, PY - 2001/7/4/pubmed PY - 2002/1/5/medline PY - 2001/7/4/entrez SP - 107 EP - 18 JF - Journal of biochemistry JO - J Biochem VL - 130 IS - 1 N2 - In order to elucidate the mechanism of the thermostability of proteins from hyperthermophiles, X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus (PfPCP), and its mutant protein with Ser substituted at Cys142 and Cys188 were determined at 2.2 and 2.7 A resolution, respectively. The obtained structures were compared with those previously reported for pyrrolidone carboxyl peptidases from a hyperthermophilie, Thermococcus litoralis (TlPCP), and from a mesophile, Bacillus amyloliquefaciens (BaPCP). The PfPCP structure is a tetramer of four identical subunits similar to that of the TlPCP and BaPCP. The largest structural changes among the three PCPs were detected in the C-terminal protrusion, which interacts with that of another subunit. A comparison of the three structures indicated that the high stability of PfPCP is caused by increases in hydrophobic interactions and hydrogen bonds, the formation of an intersubunit ion-pair network, and improvement to an ideal conformation. On the basis of the structures of the three proteins, it can be concluded that PfPCP does not have any special factors responsible for its extremely high stability and that the conformational structure of PfPCP is superior in its combination of positive and negative stabilizing factors compared with BaPCP. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/11432786/X_ray_crystalline_structures_of_pyrrolidone_carboxyl_peptidase_from_a_hyperthermophile_Pyrococcus_furiosus_and_its_cys_free_mutant_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/130.107?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -